BMRB Entry 34108
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34108
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Title: NMR structure of TLR4 transmembrane domain (624-670) in DMPG/DHPC bicelles PubMed: 28761155
Deposition date: 2017-02-28 Original release date: 2017-08-31
Authors: Mineev, K.; Goncharuk, S.; Goncharuk, M.; Arseniev, A.
Citation: Mineev, K.; Goncharuk, S.; Goncharuk, M.; Volynsky, P.; Novikova, E.; Aresinev, A.. "Spatial structure of TLR4 transmembrane domain in bicelles provides the insight into the receptor activation mechanism." Sci. Rep. 7, 6864-6864 (2017).
Assembly members:
entity_1, polymer, 48 residues, 5282.465 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MNITSQMNKTIIGVSVLSVL
VVSVVAVLVYKFYFHLMLLA
GCIKYGRG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 657 |
| 15N chemical shifts | 145 |
| 1H chemical shifts | 1098 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 48 residues - 5282.465 Da.
| 1 | MET | ASN | ILE | THR | SER | GLN | MET | ASN | LYS | THR | ||||
| 2 | ILE | ILE | GLY | VAL | SER | VAL | LEU | SER | VAL | LEU | ||||
| 3 | VAL | VAL | SER | VAL | VAL | ALA | VAL | LEU | VAL | TYR | ||||
| 4 | LYS | PHE | TYR | PHE | HIS | LEU | MET | LEU | LEU | ALA | ||||
| 5 | GLY | CYS | ILE | LYS | TYR | GLY | ARG | GLY |
Samples:
sample_1: DHPC 71 ± 1 mM; DMPG 29 ± 1 mM; TLR4-TM, [U-13C; U-15N], 0.5 ± 0.05 mM; imidazole 10 mM; sodium azide 0.01%
sample_2: DHPC 71 ± 1 mM; DMPC 29 ± 1 mM; TLR4-TM, [U-13C; U-15N], 0.5 ± 0.05 mM; imidazole 10 mM; sodium azide 0.01%
sample_3: DPC, [U-2H], 50 ± 1 mM; TLR4-TM, [U-13C; U-15N], 0.5 ± 0.05 mM; imidazole 10 mM; sodium azide 0.01%
sample_conditions_1: ionic strength: 10 mM; pH: 6.0; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_3 | isotropic | sample_conditions_1 |
Software:
CARA v1.9.1, Keller and Wuthrich - chemical shift assignment
CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation
TOPSPIN v3.5, Bruker Biospin - processing
NMR spectrometers:
- Bruker AvanceIII 600 MHz
- Bruker AvanceIII 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts